HSP90 beta protein-HIS Epitope

HSP90β is a member of the HSP90 family of proteins which are important molecular chaperones involved in signal transduction, cell cycle control, stress management, and folding, degradation, and transport of proteins (1) . HSP90 proteins have been found in a variety of organisms suggesting that they are ancient and conserved. HSP90 binds to client proteins (such as steroid receptors, AKT, Bcr-Abl, Apaf-1, survivin, cyclin dependent kinases) and acts as a molecular chaperone. Failure of Hsp90 chaperone activity leads to misfolding of client proteins, which leads to ubiquitination and proteasome degradation, and thus deregulation of cellular homeostasis (2) . HSP90β Protein is ideal for investigators involved in Signaling Proteins, Cell Stress & Chaperone Proteins, AKT/PKB Pathway, Apoptosis/Autophagy, Cancer, and Cellular Stress research. HSP90β Protein is stored in 50mM NaPhosphate pH7.0, 300mM NaCl, 150mM imidazole, 0.1mM PMSF, 0.2mM DTT, 25% glycerol. HSP90β Protein is suitable for use in Western Blot and ATPase Assay. Expect a band approximately ~91kDa on specific lysates or tissues. Specific conditions for reactivity should be optimized by the end user.